Isolation and partial amino acid sequence of A 78 kDa porcine gastrin-binding protein |
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| Affiliation: | 1. Ludwig Institute for Cancer Research, Melbourne Tumour Biology Branch, The Walter and Eliza Hall Institute of Medical Research, P.O. Royal Melbourne Hospital, Victoria 3050, Australia;2. Joint Protein Structure Laboratory, Ludwig Institute for Cancer Research, The Walter and Eliza Hall Institute of Medical Research, P.O. Royal Melbourne Hospital, Victoria 3050, Australia [Fax (61-3) 347 1938];1. Division of Rheumatology, Immunology, and Allergy, Brigham and Women’s Hospital, Harvard Medical School, 1 Jimmy Fund Way, Smith Building, Room 516c, Boston, MA 02115, USA;2. Division of Rheumatology, Immunology, and Allergy, Brigham and Women’s Hospital, Harvard Medical School, 1 Jimmy Fund Way, Smith Building, Room 626, Boston, MA 02215, USA;1. Department of Chemical and Biological Engineering, Centre for Catalysis Research and Innovation, University of Ottawa, 161 Louis Pasteur Pvt., Ottawa, Ontario, Canada K1N 6N5;2. Department of Chemical Engineering, 1280 Main Street West, Hamilton, ON, Canada L8S 4L7;1. Tianjin Key Laboratory of Food Biotechnology, College of Biotechology and Food Sciences, Tianjin University of Commerce, Tianjin 300134, China;2. Tianjin Key Laboratory for Postharvest Physiology and Storage of Agricultural Products, National Engineering and Technology Research Center for Preservation of Agricultural Products, Tianjin 300384, China;3. Institute of Agro- Products Processing Science and Technology, Chinese Academy of Agricultural Sciences/Key Laboratory of Agro-Products Processing, Ministry of Agriculture, Beijing 100193, China;1. School of Marine Science and Technology, Northwestern Polytechnical University, Xi’an 710072, China;2. Key Laboratory for Unmanned Underwater Vehicle, Northwestern Polytechnical University, Xi’an 710072, China;1. Key Laboratory for Green Chemical Technology of Ministry of Education, Collaborative Innovation Center of Chemical Science and Engineering, School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, PR China;2. Joint School of National University of Singapore and Tianjin University, International Campus of Tianjin University, Binhai New City, Fuzhou 350207, PR China;3. The Center for Advanced Mössbauer Spectroscopy, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, PR China;1. Drug Product Development, Bristol Myers Squibb, New Brunswick, NJ 08901, USA;2. Shanghai Hengrui Pharmaceuticals Co. Ltd, Shanghai 200245, China;3. Cell Therapy Brand & Franchise Strategy, Bristol Myers Squibb, Lawrenceville, NJ 08648, USA |
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| Abstract: | - 1.1. A 78 kDa protein (p78) has been partially purified from washed membranes isolated from the corpus of porcine gastric mucosa. The purification was monitored by covalent cross-linking of iodinated [Nle15]-gastrin; 17.
- 2.2. A single N-terminal sequence extending for 33 amino acids was obtained from the p78 preparation. Partial sequences totalling 192 amino acids were also obtained from 14 tryptic and 3 Staphylococcal V8 peptides.
- 3.3. 10 peptides plus the N-terminal sequence were derived from a previously unsequenced protein which was distantly related to the product of the E. coli fadB gene (Baldwin G. S. (1993) Comp. Biochem. Physiol. 104B, 55–61). The remaining 7 peptides were derived from the gb-subunit of the gastric H+/K+-ATPase.
- 4.4. The gastrin-binding activity remained in association with p78, and could be separated from the P-subunit of the gastric H+K+-ATPase, during chromatography on tomato lectin-Sepharose.
- 5.5. We conclude that p78 binds gastrin, and is a novel member of the enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase family of enzymes.
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